Eva M. Jimenez-Mateos
Spanish National Research Council
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Featured researches published by Eva M. Jimenez-Mateos.
Journal of Neuroscience Research | 2002
Christian González-Billault; M. Engelke; Eva M. Jimenez-Mateos; Francisco Wandosell; A. Cáceres; J. Avila
Several lines of evidence have indicated that changes in the structure of neuronal cytoskeleton provide the support for the dramatic morphological changes that occur during neuronal differentiation. It has been proposed that microtubule‐associated proteins can contribute to the development of this phenomenon by controlling the dynamic properties of microtubules. In this report we have characterized the effect of the combined suppression of MAP1B and tau, and MAP1B and MAP2 on neuronal polarization in cultured hippocampal cells grown on a laminin‐containing substrate. We have taken advantage of the use of a mouse line deficient in MAP1B expression obtained by the gene trapping approach. In addition to this engineered mice line we used the antisense oligonucleotide approach to induce the suppression of tau or MAP2, in wild type and MAP1B‐deficient neurons. Together these results show a synergistic role for MAP1B/MAP2 and MAP1B/TAU.
Biochemical Journal | 2006
Eva M. Jimenez-Mateos; Christian González-Billault; Hana N. Dawson; Michael P. Vitek; Jesús Avila
The MAPs (microtubule-associated proteins) MAP1B and tau are well known for binding to microtubules and stabilizing these structures. An additional role for MAPs has emerged recently where they appear to participate in the regulation of transport of cargos on the microtubules found in axons. In this role, tau has been associated with the regulation of anterograde axonal transport. We now report that MAP1B is associated with the regulation of retrograde axonal transport of mitochondria. This finding potentially provides precise control of axonal transport by MAPs at several levels: controlling the anterograde or retrograde direction of transport depending on the type of MAP involved, controlling the speed of transport and controlling the stability of the microtubule tracks upon which transport occurs.
Journal of Neuroscience Research | 2005
Eva M. Jimenez-Mateos; Gabriela Paglini; Christian González-Billault; Alfredo Cáceres; Jesús Avila
The different strains of microtubule‐associated protein (MAP)‐1B‐deficient mice that have been generated appear to express different phenotypes. This variability could be the consequence of the distinct genetic backgrounds of the animals used to generate these lines. Certain proteins might be able to complement the deficit of MAP1B function in these mice. Therefore, we examined whether the concentrations of potential compensatory proteins varied among these mutant strains. In this way, we identified significant differences in the amounts of the microtubule‐associated EB1 protein between two of these strains. Furthermore, in transfection studies, we demonstrated that the overexpression of end binding protein‐1 (EB1) could facilitate axonogenesis in MAP1B–/– cells in which EB1 is normally weakly expressed. Thus, we suggest that EB1 could complement MAP1B function during neural development.
Biochemical Journal | 2005
Eva M. Jimenez-Mateos; Francisco Wandosell; Orly Reiner; Jesús Avila; Christian González-Billault
For neuronal migration to occur, the cell must undergo morphological changes that require modifications of the cytoskeleton. Several different MAPs (microtubule-associated proteins) or actin-binding proteins are proposed to be involved in the migration of neurons. Therefore we have specifically analysed how two members of the MAP family, MAP1B and LIS1 (lissencephaly-related protein 1), interact with one another and participate in neuronal migration. Our results indicate that, in hippocampal neurons, MAP1B and LIS1 co-localize, associate and interact with each another. The interaction between these two MAPs is regulated by the phosphorylation of MAP1B. Furthermore, this interaction interferes with the association between LIS1 and the microtubule-dependent molecular motor, dynein. Clearly, the differential binding of these cytoskeletal proteins could regulate the functions attributed to the LIS1-dynein complex, including those related to extension of the neural processes necessary for neuronal migration.
Developmental Neuroscience | 2008
Elías Utreras; Eva M. Jimenez-Mateos; Erick Contreras-Vallejos; Elena Tortosa; Mar Pérez; Sebastián Rojas; Lorena Saragoni; Ricardo B. Maccioni; Jesús Avila; Christian González-Billault
Microtubule-associated protein 1B (MAP1B) is the first microtubule-associated protein to be expressed during nervous system development. MAP1B belongs to a large family of proteins that contribute to the stabilization and/or enhancement of microtubule polymerization. These functions are related to the control of the dynamic properties of microtubules. The C-terminal domain of the neuronal α-tubulin isotype is characterized by the presence of an acidic polypeptide, with the last amino acid being tyrosine. This tyrosine residue may be enzymatically removed from the protein by an unknown carboxypeptidase activity. Subsequently, the tyrosine residue is again incorporated into this tubulinby another enzyme, tubulin tyrosine ligase, to yield tyrosinated tubulin. Because neurons lacking MAP1B have a reduced proportion of tyrosinated microtubules, we analyzed the possible interaction between MAP1B and tubulin tyrosine ligase. Our results show that these proteins indeed interact and that the interaction is not affected by MAP1B phosphorylation. Additionally, neurons lacking MAP1B, when exposed to drugs that reversibly depolymerize microtubules, do not fully recover tyrosinated microtubules upon drug removal. These results suggest that MAP1B regulates tyrosination of α-tubulin in neuronal microtubules. This regulation may be important for general processes involved in nervous system development such as axonal guidance and neuronal migration.
Cell Death and Disease | 2018
Tobias Engel; Raquel Gómez-Sintes; Mariana Alves; Eva M. Jimenez-Mateos; Marta Fernández-Nogales; Amaya Sanz-Rodriguez; James Edwards Morgan; Edward Beamer; Alberto Rodríguez-Matellán; Mark Dunleavy; Takanori Sano; Jesús Avila; Miguel Medina; Félix Hernández; José J. Lucas; David C. Henshall
Glycogen synthase kinase-3 (GSK-3) is ubiquitously expressed throughout the brain and involved in vital molecular pathways such as cell survival and synaptic reorganization and has emerged as a potential drug target for brain diseases. A causal role for GSK-3, in particular the brain-enriched GSK-3β isoform, has been demonstrated in neurodegenerative diseases such as Alzheimer’s and Huntington’s, and in psychiatric diseases. Recent studies have also linked GSK-3 dysregulation to neuropathological outcomes in epilepsy. To date, however, there has been no genetic evidence for the involvement of GSK-3 in seizure-induced pathology. Status epilepticus (prolonged, damaging seizure) was induced via a microinjection of kainic acid into the amygdala of mice. Studies were conducted using two transgenic mouse lines: a neuron-specific GSK-3β overexpression and a neuron-specific dominant-negative GSK-3β (GSK-3β-DN) expression in order to determine the effects of increased or decreased GSK-3β activity, respectively, on seizures and attendant pathological changes in the hippocampus. GSK-3 inhibitors were also employed to support the genetic approach. Status epilepticus resulted in a spatiotemporal regulation of GSK-3 expression and activity in the hippocampus, with decreased GSK-3 activity evident in non-damaged hippocampal areas. Consistent with this, overexpression of GSK-3β exacerbated status epilepticus-induced neurodegeneration in mice. Surprisingly, decreasing GSK-3 activity, either via overexpression of GSK-3β-DN or through the use of specific GSK-3 inhibitors, also exacerbated hippocampal damage and increased seizure severity during status epilepticus. In conclusion, our results demonstrate that the brain has limited tolerance for modulation of GSK-3 activity in the setting of epileptic brain injury. These findings caution against targeting GSK-3 as a treatment strategy for epilepsy or other neurologic disorders where neuronal hyperexcitability is an underlying pathomechanism.
Journal of Neurobiology | 2004
Christian González-Billault; Eva M. Jimenez-Mateos; Alfredo Cáceres; Javier Díaz-Nido; Francisco Wandosell; Jesús Avila
Cerebral Cortex | 2005
Christian González-Billault; José Antonio del Río; Jesús M. Ureña; Eva M. Jimenez-Mateos; María J. Barallobre; Marta Pascual; Lluís Pujadas; Sergi Simó; Anna La Torre; Rosalina Gavín; Francisco Wandosell; Eduardo Soriano; Jesús Avila
Non-coding RNA Investigation | 2018
Eva M. Jimenez-Mateos; David C. Henshall
Archive | 2009
Eva M. Jimenez-Mateos; David C. Henshall